ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9KDJ3 | MNVFDTLQQSKKLPDVYRQMTRVELEERIRQHKERLGKKLLMLGHHYQRDEVFQFADQTGDSLQLAQIAAKEKEAQFIVFCGVHFMAETADLLTSEEQTVLLPDLRAGCSMADMADIHQTERAWERLQLMFGDTILPLTYVNSTAAIKAFCGRNGGATVTSSNAKKMLEWAFTQKERLLFLPDQHLGRNTAYELGIPLEAMAVWNPETERLETDQPLENIRVILWKGHCSVHEKFTVKHIEHLRKNEPDMSIIVHPECTHDVVIHADDAGSTHYIIKTIESADSGTKWAVGTEMNLVNRLANEHPDKEIVSLNPTMCPCL... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 41873
Sequence Length: 367
Pathway: Cof... |
Q5UXB3 | METAAFETDLSLFKYDNLEQLPPSYRDLDADERTERIESALAELGDDVVILGHNYQRQEIVEHADFIGDSYQLSKEAAQSDADYVIFGGVTFMAESADIITDDDQSVILPSMEASCPMAGMAEALQVDAAWAELTAALDDEEIIPITYMNSYADLKAFCAEQGGLVCTSSNAHKAFEYAFEKGDKVLFLPDKHLGENTAHRLGMADETVEWDPWDAEGTDAADAVENDVILWEGYCQVHERFREHHIESIREDYPDANVIVHPECRREVVEAADVAGSTSTICESVAEADPGETWAIGTEIHLTHHLQRWHPDVNVVPLC... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 41761
Sequence Length: 374
Pathway: Cof... |
Q9F364 | MTTAQTQELDVQPTPLALLLLGREADPRSERGVECPGDLPSPSDPDLVARARAAKEKLGDKVFVLGHHYQRDEVIQFADVTGDSFKLARDAAARPEAEYIVFCGVHFMAESADILTSNDQKVVLPDLAAGCSMADMATAEQVAECWDVLTEAGIAEQVVPVSYMNSSADIKAFTGKHGGTICTSSNAERALNWAFEQGEKVLFLPDQHLGRNTAVRDLGMSLEDCVVYNPHRPNGGLTAKELRDANMILWRGHCSVHGRFSLDSVNDVRERIPGVNVLVHPECKHEVVAAADYVGSTEYIIKALEAAPAGSKWAIGTELN... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 43125
Sequence Length: 394
Pathway: Cof... |
Q9L790 | MFLAADRPTTDLPADLPAAIAALKQELNAVILAHYYQEAAIQDVADYIGDSLGLSRQAAAADADVIVFAGVHFMAETAKILNPQRQVLLPDLAAGCSLADSCPPEAFAAFKAAHPNHIVISYINCTAEIKALSDIICTSSNAVKIVQQIPVDQPIIFAPDRNLGRYVMQQTGRDLVLWDGSCIVHETFSEQRLLELQARHPDAEIIAHPECETPVLDQARFIGSTTALLNYSLNSPSREFIVVTEPGIIHQMQQAAPEKTFIPAPPQDTTCACNECPFMRLNTLEKLYLCMRDRRPEIQIPEETRLAALRPIERMLAMSA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 35156
Sequence Length: 320
Pathway: Cof... |
Q9X1X7 | MVDEILKLKKEKGYIILAHNYQIPELQDIADFVGDSLQLARKAMELSEKKILFLGVDFMAELVKILNPDKKVIVPDRSATCPMANRLTPEIIREYREKFPDAPVVLYVNSTSECKTLADVICTSANAVEVVKKLDSSVVIFGPDRNLGEYVAEKTGKKVITIPENGHCPVHQFNAESIDAVRKKYPDAKVIVHPECPKPVRDKADYVGSTGQMEKIPEKDPSRIFVIGTEIGMIHKLKKKFPDREFVPLEMAVCVNMKKNTLENTLHALQTESFEVILPKEVIEKAKKPILRMFELMG | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 33617
Sequence Length: 298
Pathway: Cof... |
Q5SJM4 | MGRMRGEALAQEVLRLKRERNAVILAHSYQLPEVQEVADFVGDSLGLAREAQRTRAEVIVFCGVHFMAETAAILNPEKTVLLPDLEAGCSLADSIRPEDVLAWKAKHPDGIVVAYVNTKAEVKALADVCVTSANAVEVVSRLPQDRPIYFVPDMFLGAHVARVTGRRLDLFPGECHVHAGIREEHLKALLEAHPGAEFLIHPECGCGSGCLYLKPDAKMLSTEGMVRYAKGAEAREFVVATEVGILHRLKKEAPEKAFFPVKPDAVCEYMKRITLEKVYLSLKEMRHVVRVPEEVAGRARRALEAMVAVG | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 34181
Sequence Length: 310
Pathway: Cof... |
B5YJJ2 | MVNRTVEEILALKKQRNAIILAHNYQREEVQEIADFVGDSLELSRQATKVDCDVIVFCGVHFMAETAAILNPDKTVLLPEIDAGCPMADTVDVEELKRWIDRYPYAPIVSYVNTTAEVKALSYACCTSANAPQIVKAVPFSSIIFVPDKNLADWVKKHVPEKDIIAWNGFCPTHHMIKKEDIIRAKKAHPDALVVVHPECRPEVIELADHVASTSGMVRFARAASQKEFIIGTEVGLLYRLKKENPDKVFYPIKKTMICPNMKITTLESILTALKENQYVIKVPEDIRIKAYEAVQRMLTLIS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 34147
Sequence Length: 303
Pathway: Cof... |
B3PKM9 | MRPTLGLFGGTFDPIHIGHLRLALELKQQLQLDGMRLMPCHLPAHRDQPGASSTQRATMLQLALAACPELSIDLREVARARASYTVDSLSELRAELGAETSLVFCLGTDSFAGLDRWHRWQELLQLAHLVVVERPGWDIPSTGPVRTLLAQHQGAPGQLRLAACGSIVRLAPRLLPISATEIRQLIGAGQSPQFLVPDSVWQYIGQERLYR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23294
Sequence Length: 211
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
A3PLX6 | MVVGLLGGSFDPPHPGHVHITREALKRFGLDRVWWLVSPGNPLKPRPPAPLARRLAEARRLMRHPRVAVTGLEAEIGTRFTAETLAVLQRRYPGVRFVWLMGADNLAQFHRWERWRAIMESVPVGVLARPGAGLRARTSPAARRYASALLPEAEAARLGRSAAPAWCFVNLPMMDLSSTEIRATGRWRGQAD | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21379
Sequence Length: 192
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q3ANY3 | MHCALMGGSFDPPHNGHLALALAARELLNVECLFLSPSRNPFKGESLLDDVHRIQLVELLAKEVNRTGSGCEVCRWEIEQAAPSYTVELISYLTQSYPTWRFTLILGEDNFHSFHLWKEYQEILRLCHVAVFRRSSEAVVPSLDEAMLVQEGVSFYNFDAPLSSTDIRKQLRAGLPVNGLLPASILRYIEQEGLYR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22221
Sequence Length: 196
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
B3QLU8 | MRTGIFGGSFDPPHNGHLAMCLFARELLRLDRLIVSVSRNPFKTGAHASDDDRVSMARLLTDEVNAAGRFAESSSWELETDGPSYTVDLLRHIADLYPDDELLLLVGEDSYRQMGQWKAASEIPRLCQIVYFGREGYENCQHDAEALHLPVRRIDFDMPVSATEIRRLVAAGQPVSQLVPPSINHYIAEHGLYRS | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21910
Sequence Length: 195
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
B3EQ84 | MRLAVFGGSFDPPHNGHLALCLYARELLQVDRLVISASNNPLKDAPQAADRDRVKMAELLAETINRTGAFAEVSSWEANRGHPVYTIDLMEYLEEIYSTSDLTLLIGEDNFLNFRQWKSWEELIRRYSIIVFGRKADDGASDDSAISERLHDQSFRHIDLNLPLSSTEIRKRLASGDDCSAEIPSPIWQYIVENQLYQ | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22559
Sequence Length: 198
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
B3QYZ5 | MKKIALFGGSFDPPHYGHFALCTLTRELFSPEKIILSISKNPLKGSANAPEAHQLAMAKLMAEELGKTGPVFEVSDWELRRAGFSYTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSGTQGEQQSSRIIPPERYTWVQLDLPLSSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLYQNEK | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22562
Sequence Length: 199
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q8KGF2 | MRTAVFGGSFDPPHNGHLALSLFARELAGLDRLIVSVSKNPFKAAADASDDDRSAMARLLVAEINVAGVFAEISGWELQQSGPSYTIDLLRHVEERCPGDELVLLVGEDSYLQMPQWKFASEILKHCTIAVFGRSDIDAADAPPSDPLLPAIHYDFDMPVSATKIRRLAAAGQPIGQFVPSSIAQYIAEHKLYSA | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21163
Sequence Length: 195
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q1QXB3 | MCAAEARPARVAMLGGTFDPVHMGHLRSAVELREALELDRVHMVPARVPPHRATPGVSAERRAALLALGIGDTPGLAVDDREIARDGPSYSADTLASLREELGPQARLVMALGHDAYLNLAEWHEPQRLFDLAHIVVIDRPDHDRPLAPALQELVAGREVSDVETLMQAPAGSLLALRLPTRMAISATSIRERLRRGDSIRYLVPEAVERDLLARGLYA | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23912
Sequence Length: 219
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q7P0P7 | MNARVGVFGGTFDPVHHAHLRMARAFADELALDEVRLIPAGQPYHRLEGPHASAAQRLDMVKLAIAADARLAVDEREIRRARPAYTVDTLRELRAELGDAAELWFLIGGDSLAALSSWKDWRKLFRLANLAVAMRPGFDPAALPPEVFQEWQARQVSDFSNRTASGTIRPLALPPLDLSATRLRARLAADEPVDGLIDPAVLAYIRRQRLYR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23621
Sequence Length: 212
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
B5EEI3 | MRLGILGGTFNPIHNAHLRIAEEARDLYQLDRVVFIPAATPPHKPLVGELSFASRLEMVRLAVADNPGFMVSDMEGVRGGRSYSIDTLRELKARYPDDDLFFIVGADSFNDISTWREYEAIFELCNVISVQRPGSTITSLAEALPVAIAGEFCYDPAAKRLNHCSGHAVYALDGVLLDISSSHIRLSVQGGRSIRYLLPDAVEHYIKEQRLYVDAR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24020
Sequence Length: 216
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q49Y35 | MAKSIVLYGGQFNPIHIAHMVVASEVNAFIKPDVFYFIPSFISPLKEHTDYLEGRYRVDMIQSVIDDLGFGRICLNEIERRGQSYTYDTVMYILDKHPDAKLYLVIGTDQYNQLHKWFKINELKSYITFVIVNRDKTTQEVESEMLSITIPRIDISSTLIRKRVKNKENIQALVSPSVEQYIREEGLYES | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22148
Sequence Length: 190
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q9RDK7 | MGGTFDPIHHGHLVAASEVAAQFQLDEVVFVPTGQPWQKSHRAVSAAEDRYLMTVVATVENPQFSVSRIDIDRGGPTYTVDTLRDLRALNPDADLFFITGADALAQILTWRDSEELFSLAHFIGVTRPGHTLTDAGLPKGGVSLVEVPALAISSTDCRARVAKGDPVWYLVPDGVVRYIDKRHLYRGE | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 20581
Sequence Length: 188
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
B2FPR4 | MMSLRIYYGGTFDPVHLGHLAIARAARDELQVAVRMLPAADPPHRAVPGATADQRFTMLSLAIGDEPGLLLDHRELDRAIRFPGRPSYTVDTLRELRGELGPSRPLAWLVGADSLLGLTRWHEWEALFGLAHFVVAERPGSPLQASVDGELGRALEGRWADNEQALFASPAGRILRLHHPLREESASAVRAQIAAGGPWRALLPPAVADYVAAHGLYRSPTP | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24188
Sequence Length: 222
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q8DSI6 | MALELLTPFTKVELEEERKDKNRKQIGILGGNFNPVHNAHLLVADQVRQQLGLDEVLLMPEYKPPHVDKKATIDEKHRLKMLELAIKGIEGLAIETIELKRKGVSYTYDTMKDLIEQNPDVDYYFIIGADMVDYLPKWHKIDELIQMVQFVGVQRPKYKAGTSYPVIWVDVPLMDISSSMIRDFIRKNRKPNFLLPKLVLDYIEKEGLYQ | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24441
Sequence Length: 210
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q30PQ2 | MDTIALFGGSFDPPHIGHEAIIEALKKFKDIDKIIIMPTFLNPFKSNFYAPSSLRVKWLREIFKEEKRVEVSDYEVLQNRQVPTIETAKHLLESYKKIYLVIGADNLAKLRDWNSYDELKELVTFVVATRDDIEIPDEFIMLSVDEKISSTQLRENIQLSKLPKKCAKEIYDFYKEEHCKTE | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21320
Sequence Length: 182
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
A6QCD6 | MVNQSKPEVAIFGGSFDPPHKGHQQIVRKAVQILDIDKLIVLPAYLNPFKNVSLANPEKRLEWCYQLFDGIPKVVVDDYEIRQNKSVRTSQSVKHFNNTYSVKYLIIGSDNLSTLTKWHEFKWLNDHITWVIVTRKGHPVQTEGLKSWRILEIDFPISSTTIREKKDLRYIDNKIKQSVEKTIKDKKE | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21959
Sequence Length: 188
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q67SC4 | MARVAVLGGTFDPIHLGHLAAAQGVLHLTGVERVIFLPNRQPPHKQGQPVTPAEHRAAMVRLAIADNPAFGFSDLELRRPGPSYTIETVRALAAEHPDWEPAFIIGLDSLLAIRTWREWETLMQSVDFFAVTRPGHDLAAARRLLAELGPRLSGRVRLLEIPGVAVASADLRRLAAAGYPLRYLVPDPVARYIAEHRLYLRGESHGDG | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22845
Sequence Length: 208
Pathway: Cofactor biosynthesis; NAD(+) biosynt... |
Q8TK88 | MDFEKAQNRIIEFIRNETDKAGVDGAVVGISGGIDSALTATLTVEALGKERVLGLHMPESSLTPAVDSEDAKILADWLGIEYRTIDISGIVSAFMASIPESESSDRLTRGNLKARTRMSLLYFHANRLNRMVVGTGNKTEILLGYYTKYGDGGVDLEPIGGIYKTEVWELSRRLGIPDPLITKKPSAGLWTGQTDEAELGISYLKVDDVLRMIEEGAEQEKILKDTGISIEQLNSVTRRIERNEHKRKSPPVPELY | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28295
Sequence Length: 256
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
A7IAS7 | MAQELGCRMGQVEQMIRYAYWNSKSQGIVVGVSGGVDSALAAAFCCRAIGPEKVLGLSLPASVSNPQDLSDAQELCAMLGMEHRVVLIDPMLAAFKTIPGFVETPYLLGNLMARIRMTVLYYHANRDHRLVCGTSNRSEAMLGYCTKYGDNAADFQPIVHLYKTDVYEMAKEVKIPKAILEKTPSAGLWAGQSDEGEIGLSYAEIDAALKNLEANGWKAGTPSEEKVLSRAQANAHKRLAAPNLLSVP | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 26893
Sequence Length: 248
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
Q12V31 | MDIIQAKDIIIDFIGTKLEGTGIEGAVVGISGGIDSALVAYLSVEALGAENVLGIHMPEASTPKSEIEDASKVAEALGIDFKVINITNVLEVYRTAMPDIDGASAHVDGNLKARIRMSMLYYYANMFGRVVMGTGNKSEILLGYFTKYGDGGVDIEPIGDLYKTEVREMSKMLGVPESILEKAPSAGLWEGQTDEDDLGVTYETIDKVLQPILAGEGQERVHLKLGVPMEEISSILLRVRSNLHKRTTPQIAYLDDLRGDWLS | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28578
Sequence Length: 263
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
Q58747 | MLWGESMEEIVNKITKFIREKVEEANANGVVVGLSGGIDSSVTAYLCVKALGKDKVLGLIMPEKNTNPKDVEHAKMVAENLGIKYIISDITDILKAFGAGGYVPTREFDKIADGNLKARIRMCILYYFANKYNLLVAGTSNKSEIYVGYGTKHGDIACDIRPIGNLFKTEVKKLAKYIGVPKEIIEKPPSAGLWEGQTDEEELDIKYETLDTILKLYEKGKTPEEIHKETNIPLETINYVFDLIKKNEHKRTLPPTPEI | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28982
Sequence Length: 259
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
Q8TVH1 | MAKYEPVIPELEVNPEGEVSKIAEFLRGKFEEAGREIAVVGLSGGVDSSTTLGLAVEALGRENVVALILPERDTPEEDVEDAVEAAERFGVEYHVHDITEVLRAFGTGSYVPCHPFSRKSDANLKPRVRMCVLYYFANELDGLVLGTGNRTEWLTGYFTLHGDGACDVAPIRHLYKTQVYVIAEHLGVPERIVEEKEPSARLWPGQTDEGELGIDYPTLDALLYALVDEGLGPRKAVDWLGERGVEATEEDAEKVLDLVRSSSFKRRPAPGLDLPEPEDPAMSG | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 31191
Sequence Length: 284
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
O27554 | MKCVPGLCSEVVSVIEDFIRQKVAESGASGVVLGLSGGVDSSTVAYLAVNALGPDRVLGLIMPSSTTPRDDLRHARTVADELGIESETIDIDPIIESLTGLCSHNANELALANLKPRARMVILYYHANSLNRLVAGTGNRTELLLGYFTKYGDGGVDMLPIGGLYKGQVRELAGRLGVPPEIIKKPPTAGLWHGQTDEEELGMKYDLLDELLCLLVDRKLPVEEVASTLSLPPSEVERIASMVKGSEHKLKPPEVPDIWEVMECSH | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28722
Sequence Length: 266
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
P0A5L7 | MNFYSAYQHGFVRVAACTHHTTIGDPAANAASVLDMARACHDDGAALAVFPELTLSGYSIEDVLLQDSLLDAVEDALLDLVTESADLLPVLVVGAPLRHRHRIYNTAVVIHRGAVLGVVPKSYLPTYREFYERRQMAPGDGERGTIRIGGADVAFGTDLLFAASDLPGFVLHVEICEDMFVPMPPSAEAALAGATVLANLSGSPITIGRAEDRRLLARSASARCLAAYVYAAAGEGESTTDLAWDGQTMIWENGALLAESERFPKGVRRSVADVDTELLRSERLRMGTFDDNRRHHRELTESFRRIDFALDPPAGDIGLL... | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 74683
Sequence Length: 679
Pathway: Cofactor biosynthesis; NAD(+) biosynth... |
P47623 | MTNLIKYLKELQNWLFDYVKKSKAKGVIFGLSGGIDSAVVAAIAKETFGFENHLALIMHINNSKLDFQATSELVKKMQFNSINIELEESFNLLVKTLGIDPKKDFLTAGNIKARLRMITLYAYAQKHNFLVLGTGNFVEYTLGYFTKWGDGACDIAPLAWLLKEDVYKLAKHFNIPEIVITRAPTASLFEGQTDETEMGITYKELDQYLKGDLILSSEKQKIVLDLKAKAEHKHNSPLKFKHLYNFQN | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28190
Sequence Length: 248
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
Q9CBZ6 | MDFYNSYSQGFVRVAACTHHASIGDPTTNAASVLRLARQCHDDGVAVAVFPELTLSGYSIEDILLQDLLLEAVEDTVLDIVVASADLLPVLVIGAPLRYRHRIYNTAVIIHRGVVLGVAPKSYLPTYREFYERRQLAPGDDEHGTIGIGDLRAPFGPDLLFAAADLLGLVLHVEICEDMFVPVPPSAEAALAGATVLANLSGSPITIGRAEDRRLLARSASLRCLAAYVYAAAGEGESTTDLAWDGQTMIWENGVLLAESERFPKGEHRSVADVDTELLRSERLRMGTFNDNRRRHRALVEPFRRIEFRLEPPVGNIGLL... | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 75543
Sequence Length: 680
Pathway: Cofactor biosynthesis; NAD(+) biosynth... |
Q98PU6 | MKSNTEIYKNLKLLEDYGTYLIEWIKLKVQQANKKGVIVGISGGIDSALVACLAKKAFPENSLGITMPIGNSMKLDFDDIAKLQKLTKLEIINIDLTLSYDALAKTLDVKNKLAKANIKPRLRMASLYAMAQEKDYLVLGTDNLDEWYLGYFTKYGDGGVDLLPISYLTKSEVISLAQIYKVDKGIIEKKPSAGLWENQEDEKELGYSYSEVDLFLRKKQIDSQIATKIEKQHQMTEHKRQLASKPMDIVDFENKER | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 29182
Sequence Length: 257
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
Q5YRN0 | MASLREQIITELGVQPVIEPKTEVRRRVDFLKDYLRSTPAQGFVLGISGGQDSTLTGRLCQLAAEEVRAEGGEATFVAVRLPYGVQADEHDAAVAMEFIGPDRAVTVNVKPGVDATAGAVAEGLGLDALRDFVRGNIKARERMIIQYAIAGQENLLVVGTDHAAEAVTGFFTKYGDGGVDLTPLTGLTKRQGAALLQELGAPPSTWSKVPTADLEDDRPALPDEEALGLRYSEIDDYLEGKEVTEAVAARVEQLYTATRHKRTVPVSPLDSWWR | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 29601
Sequence Length: 274
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
A2YII8 | MRLLRVATCNLNQWAMDFDTNLRNVKESIARAKAAGAAVRVGPELELTGYGCEDHFLEQDTAAHAWECLKDILSGGYTDGILCSIGMPVIFKSVRYNCQVFCLNSKIVMIRPKISLANDGNYREFRWFSAWTFKDALVDFQLPLDISEVTSQDTVPFGYGFIQFLDVSLASETCEELFTANAPRIDLALNGVEVFVNASGSHHQLRKLSLRIDSMRNATLACGGVYMYANQQGCDGGRLYYDGCCCIAVNGDVVAQGSQFSLKDVEVLDALVDLDAVSSYRASVSSFREQASHRTKVPFVKVPYKLCKPFQSGMVPTGPV... | Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 82077
Sequence Length: 735
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
|
Q7MAJ5 | MTLTNPSALVNQLVDFLRQELAQRGFKKVVVGLSGGVDSAVVARLCQEAIGENLHALLMPSSVSSKESVEHALLLCERFNLSHHIQSIAPLELAFRELHPEATPLRIGNACARFRMITLYDFSFKENRLVIGTGNKSEILLGYGTLYGDTACALNPIGDLYKTEIFQLAKFLSIPDEIIQKAPSADLFEGQSDEKELGFSYNDMDQLLFDHIELKLSKEELLAKGHAKELVEMVLKRISTNKFKSEMPPIAQVRGRL | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28616
Sequence Length: 257
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD... |
Q9PC24 | MSEFLRIAMAQFDFPVGAVAQNAERIIALIEQARDEHGADVVMFPELALSGYPPEDLLLRPGFLAHCQVAIERIAAATHGIVAVVGWPQSAGSVVYNVASVLCDGQVEQTYRKRELPNYAVFDERRYFEVDPNGSRCVFKVKGVPVGVLICEDLWFSEPLADTVCGGAELVLVPNASPYERGKHAQRDALLAERARETGAAIAYLNVVGGQDALVFDGASVVVDGHGRVHPAAAAFSDQWLVVDYMRSERRFVPLQWVAESEVSINALVWRAVVRGVQDYCRKNGFSKVWVGLSGGIDSALVLAIAVDALGADQVTAVRL... | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 59261
Sequence Length: 545
Pathway: Cofactor biosynthesis; NAD(+) biosynth... |
P38795 | MSHLITLATCNLNQWALDFEGNRDRILQSIKIAKERGARLRVGPELEITGYGCLDHFLENDVCLHSWEMYAQIIKNKETHGLILDIGMPVLHKNVRYNCRLLSLDGEILFIRPKIWLANDGNYREMRFFTPWMKPGVVEDFILPPEIQKVTGQRLVPFGDAVINSLDTCIGTETCEELFTPQSPHIAMSLDGVEIMTNSSGSHHELRKLNKRLDLILNATKRCGGVYLYANQRGCDGDRLYYDGCALIAINGTIVAQGSQFSLDDVEVVTATVDLEEVRSYRAAVMSRGLQASLAEIKFKRIDIPVELALMTSRFDPTVC... | Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 80686
Sequence Length: 714
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
|
Q500Y9 | MAIRKLLLLLKPIDPYPFLQTEGASLIKNPQVLQYLESRCKVHKNAIKFCQEILSKKPVEWKPISRNDLSHPIRDVDMVITVGGDGTLLHASHFIDDSVPVLGVNSDPTQAHEVEELSDQFDASRSTGHLCAATVENFEQVLDDILFGRVVPAKVSRISLKLNSETLLSHALNDILIAQPCPAAVSRFSFKIKNKDGASSPKTVNCRSSGLRICTAAGSTAAMQSAGGFVMPMLSRDLQFMVREPISPGSTASLMHSTFKPDQFMDVNWYSDHGTIYIDGCQVQHSVQLGDTIEISSDAPVLNVFLSHGISQIRSRY | Function: Phosphorylates specifically NADH. Can phosphorylate NAD with a 100-fold decrease in efficiency compared to NADH. Prefers ATP as nucleoside triphosphate substrate. Can also utilize UTP, GTP and CTP. Key source of the cellular reductant NADPH which is an important antioxidant factor.
Catalytic Activity: ATP + N... |
Q6EQG2 | MALRRVLLFVKPFDVYPPRPLAAAASSPPPPPPPLRVSNPKVLNYLDDRCRVHKETINLCKSVLQRKSIDWISVQRNDMSNPIHDVDLVISVGGDGTLLRASHFLNSSIPVLGVNSDPTCPDEVDELTDEFDARRSTGHLCAATAANFEQILDATLDGSRQPSELSRISVKLNGLQLPTYALNDILVSHPCPASVSRFSFRKRSNTGESSHLINCRSSGLRVATPAGSTAAMLSAGGFVMPISSHELQYMIREPISPRDADKPLLHGLVKQGQHILVVWYNEEGAVYFDGSHVMHSIQHGDTLEISSDAPILKVILPENL... | Function: Key source of the cellular reductant NADPH which is an important antioxidant factor.
Catalytic Activity: ATP + NADH = ADP + H(+) + NADPH
Sequence Mass (Da): 35517
Sequence Length: 325
Subcellular Location: Cytoplasm
EC: 2.7.1.86
|
Q56YN3 | MSSTYKLNHTDSFANGDAKSLLPNPENGFTHLTSLAQSEKAVQELLLQQTPMQATDDHLVEFSEALRTVAKALRGAAEGKALAQAEAAEWKRRYELERSKNVELQHKELSNGVCADESNGQRMEHLAKSPRLYAQEISSNGMETICSHEVLQDGGFNSFNNKLKRKASFKLSWGCKGMANDQHKKEIVSFERGNISTAERSSKQISLTWESDPQTVLIITKPNSTSVRVLSVDMVRWLRTQKGLNIYVEPRVKEELLSESSSFNFVQTWEDDKEISLLHTKVDLLITLGGDGTVLWAASMFKGPVPPIVPFSMGSLGFMT... | Function: Phosphorylates both NAD(+) and NADH, with a twofold preference for NADH. Source of the cellular reductant NADPH which is an important antioxidant factor.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 58245
Sequence Length: 524
EC: 2.7.1.23
|
A7ZQ55 | MNNHFKCIGIVGHPRHPTALTTHEMLYRWLCTKGYEVIVEQQIAHELQLKNVKTGTLAEIGQLADLAVVVGGDGNMLGAARTLARYDIKVIGINRGNLGFLTDLDPDNAQQQLADVLEGHYISEKRFLLEAQVCQQDCQKRISTAINEVVLHPGKVAHMIEFEVYIDEIFAFSQRSDGLIISTPTGSTAYSLSAGGPILTPSLDAITLVPMFPHTLSARPLVINSSSTIRLRFSHRRNDLEISCDSQIALPIQEGEDVLIRRCDYHLNLIHPKDYSYFNTLSTKLGWSKKLF | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 32566
Se... |
Q8EGS1 | MTTKFHTIGLIGKPHHPGTNQTLKRLHHWLTMQGYEVLVEERVATELGPHIVAVDLLEIGERCDLAIVVGGDGNMLGAARVLARFEVGVIGVNRGNLGFLTDLPPDAFEEALAKVLDGEFDTEHRFLLEAEVYRHGQLKASNTAVNEAVLHPGKIAHMIEFEVYIDNQFMYSQRADGMIVSTPTGSTAYALSAGGAILTPNLQALILVPMFPHTLSCRPIVVDACSTIKMVVSPENGENLEVSCDGHVHLAVLPGDEIIVRRSSEQLRLIHPKGHNYFHVLRSKLGWGSKLF | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 32019
Se... |
Q02A16 | MPIIKTAGIISKPNSTAAEEIVPKLIEWLRRRGIAVRIDEQTSLYSGGVSGMPREEVPQSCDLVVVLGGDGTLLSAARAIGRREIPLFPVNLGGLGFLTAISIEELYPELERALRGEHRIAKRKLMTTEVIRENNVIASFDALNDAVLTKSSIARMIDLDTYVDEQFVCAYKADGLIIATPTGSTAYSLSAGGPIIFPSVPAICLTPICPHMLTNRPVLVPETSVIRVASRGPDESVYLTIDGQVGTPIREHDTVVCHSSHHSLLLIRPPRMMFFDVLRQKLKWGER | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31420
Se... |
P34480 | MLPRKLKIDSTELAEITNELVQFLNCLVLRSGGLKKEHIWVRNGRILDERTVFFEEKTMADVQIDCEGLILSPGFIDLQLNGGFGIDFSTYNSDDKEYQEGLALVAKQLLAHGVTSFSPTVITSSPETYHKILPLLKPSNASSEGAGNLGAHLEGPFISADKRGCHPEQLVITSLSPNPVEIIEHVYGSTENIAIVTMAPELEGAQEAIEYFVSTGTTVSVGHSSAKLGPGEMAVLSGAKMITHLFNAMQSYHHRDPGLIGLLTSSKLTPDHPLYYGIISDGIHTHDSALRIAYHTNSAGLVLVTDAIAALGMSDGVHKL... | Cofactor: Binds 1 divalent metal cation per subunit.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Mass (Da): 44887
Sequence Length: 418
EC: 3.5.1.25
|
Q6P0U0 | MPSNKSVSDAPITQFVNCRILKNHKLQWEDLWVREGKILNPEKLFFDEQGFADHRVDCENKIIAPGFIDVQLNGGYGIDFSQASSDIRGGVALVAKKILEHGVTSFCPTLVTSPPHIYHKVIPELRVQDGGPEGAGVLGIHLEGPFISEEKRGAHPPKFLRTFQSGGVADLMETYGQLENVAMVTLAPELTNSAAAIHELSSRGITVSVGHSMADLSQAEEAVQNGATFITHLFNAMLPFHHRDPGIVGLLTSDRIPPGRTVYYGMIADGIHTHPAALRIAHRAHPAGLVLVTDAVTAMGLPPGRHTLGQQQIDIQGLHA... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Ma... |
Q9VR81 | MDVRIKCNSEEPESPEQKILASSQRLLQFTNCRLVRDHRIIHDDLWVRDGRIVNPEPVFFDERTKAHCRIDCGGAIIAPGYIDLQINGGYGVDFSYDTETIEEGVATVARGLVKSGVTSFCPTLVTSPSDSYHTILPRIPAEVPKGAGILGIHAEGPFINPQKKGAHPEHCIQTIDKGLSTLKETYGSLERIKIITLAPEKVTDPEVIGQLVERGITVALGHSMASLSDGERAVQQGATLITHLFNAMLPFHHRDPGLVGLLASDAVPHGRTVYFGIISDGVHTHPAALRIAYRTHPQGLILVTDAISALGLEEGVHHIG... | Cofactor: Binds 1 divalent metal cation per subunit.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Mass (Da): 45283
Sequence Length: 417
EC: 3.5.1.25
|
P0AF19 | MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQLNGCGGVQFNDTAEAVSVETLEIMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLAKHPNQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALVDFLCENADVITKVTLAPEMVPAEVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEADIYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVRNL... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate. Can probably also catalyze the ... |
P44537 | MKYALINCVIYTKYDVLRDFAVIINGEIIEAVIPQAELETGIKTIDLQGNNLTAGFIDLQLNGCGGVMFNDQTSVETLEIMQETNLKSGCTSFLPTFITAPDENIKSAVKIMREYLNKHKNQALGLHIEGPYLSIEKKGVHRPEYIREITPEMKDFLCENGDVITKMTIAAENPTINYTPDFVKAGIIVSVGHSNATYEVAKAAFHKGATFATHLHNAMSPISSGREMGVVGAVLDSDVYTGIIVDGVHINYGNVRIDKKIKGDKLCIVTDSIAAAGAPPELESFTFVGKTIYIKEGRCYDANDTIAGASITMMESIKNA... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate.
Catalytic Activity: H2O + N-ace... |
Q9Y303 | MRGEQGAAGARVLQFTNCRILRGGKLLREDLWVRGGRILDPEKLFFEERRVADERRDCGGRILAPGFIDVQINGGFGVDFSQATEDVGSGVALVARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDLLATYGPLDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVGLLTSDRLPAGRCIFYGMIADGTHTNPAALRIAHRAHPQGLVLVTDAIPALGLGNGRHTLGQQEVEVDGLTA... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present... |
Q84F86 | MFFLSLIIRNITVVNASGRDEQMDVWMKDGKIAQIAQHIHAQGVDQLEGSGKFLLPGFIDMHIHGSAQMDTMDASDEGLHIHGPITIKEGTTSFLATTMTQSFDWFDRAQRQCGNNFSPKSDEAEVLGLHIEGPFVSKQRAGAQPLDYIVQPDMEVIKKWQALSGQKIKQITLAPEEPNGMAAVQSLSESGVIVSIGHSDATFEQMQEAVQLGASQGTHLYNQMRPFHHRDPGVVGGVLLVDAIKAELIVDFIHMHEGAVEMAYRLKGADGIILITDAMRAKGMPYGEYDLGGQLVHVTESGAHLSNGSLAGSILTMDQA... | Cofactor: Binds 2 divalent metal cations per subunit.
Function: Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate.
Catalytic Activity: H2O + N-ac... |
Q8JZV7 | MRSGQCAAGAPVLQFTNCRILRGGTLLREDLWVRGGRILDPEKLFFEERRVADEQRDCGGRILAPGFIDVQINGGFGVDFSKATEDVGSGVALVARRLLSHGVTSFCPTLVTSPPEVYHKVLPQIPVKSGGPHGAGVLGVHLEGPFISREKRGAHPEAYLRSFEANAFHDVLATYGPLDNVCIVTLAPELDRSHEVIQALTAQGIRVSLGHSVADLRAAEVAVQSGATFITHLFNAMLPFHHRDPGIVGLLTSDQLPPGHCIFYGMIADGIHTNPAALRIAHRAHPQGLVLVTDAVPALGLGNGRHTLGQQEVEVDGLIA... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Ma... |
O32445 | MYALTNCKIYTGNDVLVKHAVIINGDKIEAVCPIESLPSEMNVVDLNGANLSPGFIDLQLNGCGGVMFNDEITAETIDTMHKANLKSGCTSFLPTLITSSDENMRQAIAAAREYQAKYPNQSLGLHLEGPYLNVMKKGIHSVDFIRPSDDTMIDTICANSDVIAKVTLAPENNKPEHIEKLVKAGIVVSIGHTNATYSEARKSFESGITFATHLFNAMTPMVGREPGVVGAIYDTPEVYAGIIADGFHVDYANIRIAHKIKGEKLVLVTDATAPAGAEMDYFIFVGKKVYYRDGKCVDENGTLGGSALTMIEAVQNTVEH... | Cofactor: Binds 1 divalent metal cation per subunit. Ni(2+) ion is seen in the structure.
Function: Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and ace... |
P96166 | MESKSHAHCFRAQRVLHGKQWQQDAVVTVDENGTISAIESYDGQRHADAIPLGPVDLMPGLIDSHVHGSQGCDVMDATHDSLNTMSRYFATLGVTAFVATTVTAPVAKIRAALAQVAKSKHDGVDGAEILGAYLEGPYFTEKNKGAHPTQWFRELAVEELEDWISYSDNQLLKVALAPEKTGALDAIRYLDAHGIHVMLGHSDADYEQVKAALAAGAKGIVHCYNGMRGLHHRDPGVVGAGLLHPHCFVEMIADGHHVHPAAIDVAHRCCGSRMTLITDAMRATGMPDGQYTLGEYQVDMKQGVVMTSSGGLAGSTLTLL... | Cofactor: Binds 2 divalent metal cations per subunit.
Function: Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate.
Catalytic Activity: H2O + N-ac... |
A9NEX8 | MKINVFETKEELYRAVADFYIKAINEKPNMTLGLATGTTPIPLYQNLIKAYQDKLVSFKDITTFNLDEYIGLPKTHKESYFSFMRNQLFNHVDINLDNTHIPSGVLEPSEAIKEFQTALDAHQIDIQLLGLGSNGHIGFNEPGTSFESTTHKTQLALSTIQDNSRMFDSIDEVPTESITMGIKDIMRASKIVMIATGAQKADAVYKMIQGPVDESLPASILQKHDDVVIFLDKDAASLLK | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 26786
Sequence Length: 240
Pathway: Amino-sugar met... |
Q8CTR3 | MKIINLDSKNLASFYVACELFKQIQQHPHAKLGLATGGTMTDVYHYLVNLLIKNKVDVSQVETFNLDEYVGLKASHQQSYHTYMNKVLFEQYPHFVKNHIHIPDGLSENLEAEAERYNNLLDERGPIDIQILGIGENGHIGFNEPGTDFNSETHVVNLTESTIKANSRFFDNEKDVPRQAVSMGVKSILKAKRIILLAFGPKKKEAISKLLNEQVTEDVPATILHTHPNVEVYVDDEAAPDCL | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 27383
Sequence Length: 243
Pathway: Amino-sugar met... |
Q9K487 | MEVVIVPDAKAGGELIAEAMAQLLRRKPDALLGVATGSTPLPVYEALAAKVRSGAVDTAQARIAQLDEYVGLPAEHPESYRSVLRREVLEPLGIDMDAFMGPDGTAADVQAACEAYDTALGGSGGVDLQLLGIGTDGHIGFNEPCSSLASRTRIKTLTEQTRIDNARFFDGDIEQVPHHVITQGIGTILEARHVVLLATGEGKADAVAASVEGPVAAVCPASALQLHPHATVVVDEAAASKLKLADYFRHTYAHKPDWQGI | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 27446
Sequence Length: 261
Pathway: Amino-sugar met... |
Q8DV70 | MKTIKVKNKTEGSKVAFRMLEEEITFGAKTLGLATGSTPLELYKEIRESHLDFSDMVSINLDEYVGLSADDKQSYAYFMKQNLFAAKPFKKSYLPNGLAADLAKETEYYDQILAQYPIDLQILGIGRNAHIGFNEPGTAFSSQTHLVDLTPSTIAANSRFFEKAEDVPKQAISMGLASIMSAKMILLMAFGEEKAEAVAAMVKGPVTEEIPASILQTHPKVILIVDEKAGAGI | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 25473
Sequence Length: 233
Pathway: Amino-sugar met... |
Q5XBG4 | MKIIRVQDQIEGGKIAFTLLKDSLAKGAKTLGLATGSSPISFYQEMVKSRLDFSDLTSINLDEYVGLSVESDQSYDYFMRQNLFNAKPFKKNYLPNGLATDVEAEAKRYDQIIAEHPIDFQVLGIGRNGHIGFNEPGTSFEEETHVVDLQESTIEANSRFFTSIDDVPKQAISMGIASIMKSKMIVLLAFGQEKADAIKGMVFGPITEDLPASILQKHDHVIVIVDEAAASQLD | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 25823
Sequence Length: 234
Pathway: Amino-sugar met... |
Q9UK23 | MATSTGRWLLLRLALFGFLWEASGGLDSGASRDDDLLLPYPRARARLPRDCTRVRAGNREHESWPPPPATPGAGGLAVRTFVSHFRDRAVAGHLTRAVEPLRTFSVLEPGGPGGCAARRRATVEETARAADCRVAQNGGFFRMNSGECLGNVVSDERRVSSSGGLQNAQFGIRRDGTLVTGYLSEEEVLDTENPFVQLLSGVVWLIRNGSIYINESQATECDETQETGSFSKFVNVISARTAIGHDRKGQLVLFHADGQTEQRGINLWEMAEFLLKQDVVNAINLDGGGSATFVLNGTLASYPSDHCQDNMWRCPRQVST... | Function: Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyltransferases... |
Q8BJ48 | MAAPRGPGLFLIPALLGLLGVAWCSLSFGVSRDDDLLLPYPLARRRPSRDCARVRSGSPEQESWPPPPTNPGASHHAAVRTFVSHFEGRAVAGHLTRVADPLRTFSVLEPGGAGGCAQKRRATVEDTAVPAGCRIAQNGGFFRMSTGECLGNVVSDGRLVSSSGGLQNAQFGIRRDGTIVTGYLSEEEVLDPVNPFVQLLSGVVWLIRNGNIYINESQAIECDETQETGSFSKFVNVMSARTAVGHDREGQLILFHADGQTEQRGLNLWEMAEFLRQQDVVNAINLDGGGSATFVLNGTLASYPSDHCQDNMWRCPRQVS... | Function: Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyltransferases... |
Q84JF4 | MTERGAMVVSSSTCYVPFRCPQARKDFAFVEPSKKLNPNRVLIKPPVYTYSPALTAAKCNIFDYAETGENLVGDKQFVRWFREAWPYLWAHRSCTFVVTISGDVLDGPYCDLVLKDIAFLHHLGIKFVLVPGTQVQIDQLLAERGREPTYVGRYRVTDSASLQAAKEAAGAISVMIEAKLSPGPSIYNIRRHGDSSRLHETGVRVDTGNFFAAKRRGVVDGVDFGATGLVKKIDVDRIRERLDSGSVVLLRNLGHSSTGEVLNCNTYEVATACALAIGADKLICIMDGPVLDENGHLVRFLTLQEADTLVRKRAQQSEIA... | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 67179
Sequence Length: 609
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellul... |
B5X4Z4 | MERGALVGSSSTSSYYVPYHFRQSKSNFSSFKPKNKLNPTQFRFNCSWFKPVSSITAAKCNMFDYAVTAAGDVEAEHPVDDKQFVRWFREAWPYLWAHRGCTFVVIISGEIIAGSSCDAILKDIAFLHHLGIRFVLVPGTQEQIDQLLAERGREATYVGRYRVTDAASLQAAKEAAGAISVMLEAKLSPGPSICNIRRHGDRSRLHDIGVRVDTGNFFAAKRRGVVDGVDFGATGEVKKIDVDRICERLDGGSVVLLRNLGHSSSGEVLNCNTYEVATACALAIGADKLICIMDGPILDESGHLIHFLTLQEADMLVRKR... | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 67395
Sequence Length: 613
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellul... |
Q75A07 | MLFRRLLTTKVGYHTPNYVNRRLILSVLKSTATRREAKDYLTKYGDPAVAYHCVLYLRGTKTFSAGLINDFAIMLGRLRLLGIRPLVVLSPSKHVMTESEILRETFYKHGLQSIPINEPMASGTRETILQNGASYNSIIPIIMPFVYHQQRAKRMLAEDEVAFMRELVAYMPCRIDKFFIINRYGGIPSSERHDNSHVFVNLSQEYGSLAEVLKQQITDLRHEMDDGLLAERRATDGSYKEFQYTTLTESLTDLELMSAVLSLLLPSSTGLITSMHSAVTNSRYNPLLYNVLTDRSLVSSSLPSFKRDPISDNAWYELPA... | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 61904
Sequence Length: 542
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellul... |
A2QGF0 | MSSRTLVGLRSTTSTHLQRSGVAAAAAVSSSSTSSSGSAPRRCLSSASGRQVQQSAEFSSSSKSWDRLGRRAKEKLLDREFFLSLLNSASTKREAKSYLARLKAQHQGTPPLKPAAKQPGVAEAAAPVSSGASSTSFYGASRSVYDSPVFRHDSTPTPPLQDVSERLHLALVKITTPQLLDDSTVNGVAKTLSQLNRLGMACCVVVDPGTAGDSNQLRRIAAEQADRISTAVDAQPDSKSAHIDSVLSVSALNPEAPKVLSRKLLLGPLRDGHIVVLAPIAYTEDVPRAVTVSASDAILALTKELAGLATNPDPDEDPIR... | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 78172
Sequence Length: 726
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellul... |
A6SG85 | MLLQNLALKKGKEAAGHNIQSLTKHGNYFVQSSDRRRAYTSNQSAADKVREELAKETCEKLSSQHQAKKKAKAIDRDFFLSVLGSSATKREARSYIQNFKPLNTSPAKPISQEPVHKNTNENGANLGSIYTATRAVAESPKFVQQPAVSQSTLGGSILHVALVKVRAPQLLDDETLNGIGKTLSKLCRLGLISTVVVDCEDGTDTHLKVSECEWRNRIKEQAARVVTAIDASGTEARLVDNVIGIAEDGSDVKQQPYLKGGVHVTFRELLMTPLRRGVLPVLPSIGHTDATQTAVSITASDVVLALTREFAGFRSPQSPD... | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 81144
Sequence Length: 734
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellul... |
Q59MB6 | MSKLKTLNRQFISNLETHKVTTDAKRNLILSILKSTTTKREAKNYLTKYQNQFDFNDDLDFNKSIKIKNEQSSLTNRDSQRELFINRFLNQSNPFINVYDKEDVKLQKVPLRLAIFKIKFTKITIKQWKGIAETFKRLITLGISPIIMLDYDHLPSDSYKNNELYMINQGNKMLNYLGHPEEESDLKVTLLRSLFTSHKGVPTLDSLESILIPLYQGIIPIIQPIVYNADLSKQEFLASDKLLLGLSSALIEKRTTDLLSIEKIVMIDPIGGIPSIERHQTSHVFINLSQEYSDILSELFIGHIEPKYRDTHVDNLNTMN... | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 66683
Sequence Length: 580
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellul... |
Q1DNE1 | MSRSTVLGWCTQSCRLLQKHDHSFSFPTFNGSPPLKKRRFCDSAAPAAPRPSIHRPSEYIPHSKSGGEAPQDLGHKAREKEAEKEFYLSLLCSASTKREAKSYLSRFKAQKTTANDGCQHITPRRGDLISDLELMKDKPGVNLGSMFSETRTVAETPAPKQEWSSAQSTELFREKIHVALVKLRKPQLLDDQTLHGVAKTLVQLSRLGMSCCIVIDVGTDKDETHRRIIAREQADRLSAVIDANHGPDSRQLDSIITVPSATDMKLSVLSRGPLLSPLQQGHVVVVVPVGYANDTQRAVLLPANEVVFALSKELAGLELR... | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 81514
Sequence Length: 737
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellul... |
O75011 | MENNTASSPYTKLELVGRGSYGAVYRGICNLTKETVAIKILNLDTDEDEVSDIQKEVAVLSELKQSDVENIIKYHGSYLVGTNLWIIMDYCHGGSVRTLMEAGPISEPCISLILRETLQALKFIHHAGIIHRDIKAANILVSMSGNVKLCDFGVAAELNINRRKRITFIGTPYWMAPEVIRDGQEYNVMADIWSLGITAYEIATGSPPHAKEDPFRAVYLIAHTAPPRLNGNFSALLKEFIASCLQDVPQRRLDSSELLKSKFIKQYSRMSISELTNVVKRYDTWQAAGGIPQTLLLGEEADDGSDPDQETSDTAASDDG... | Function: Has a role in the regulation of cell polarity, growth and division.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 71120
Sequence Length: 652
Subcellular Location: Cytoplasm
EC: 2.7.11.1
|
Q4G0N4 | MTCYRGFLLGSCCRVAGGRAAALRGPGAGGPAARPRLGGDGGGRRHLGQGQPRELAGCGSRADGGFRPSRVVVVAKTTRYEFEQQRYRYAELSEEDLKQLLALKGSSYSGLLERHHIHTKNVEHIIDSLRNEGIEVRLVKRREYDEETVRWADAVIAAGGDGTMLLAASKVLDRLKPVIGVNTDPERSEGHLCLPVRYTHSFPEALQKFYRGEFRWLWRQRIRLYLEGTGINPVPVDLHEQQLSLNQHNRALNIERAHDERSEASGPQLLPVRALNEVFIGESLSSRASYYEISVDDGPWEKQKSSGLNLCTGTGSKAWS... | Function: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor. Also has weak NADH kinase activity in vitro; however NADH kinase activity is much weaker than the NAD(+) kinase activity and may not be relevant in vivo.
Catalytic Acti... |
Q8C5H8 | MTCYRGFLLGSCRRVAGGRAALRGSGSGADGRRHLGHGQPRELAGGGSPADGGFRPSRVVVVAKTTRYEFEQQRYRYAELSEEDLKQLLALKGSSYSGLLERHHIHTKNVEHIIDSLRDEGIEVRLVKRREYDEETVRWADAVIAAGGDGTMLLAASKVLDRLKPVIGVNTDPERSEGHLCLPVRYTHSFPEALRRFSRGEFRWLWRQRIRLYLEGTGINPTPVDLHEQQLSLNQHSRAFNIERAHDERSEASGPQLLPVRALNEVFIGESLSSRMPYCWAVAVDNLRRDIPNLKGLASYYEISVDDGPWEKQKSSGLNL... | Function: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor (By similarity).
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 50859
Sequence Length: 452
Subcellular Location: Mitochondrion
EC: 2.7.1.23
|
Q08CZ6 | MSLCLRLLCSVCGAAALRVPLGVSSLRALSGSAEGFRPARVAVVAKTTRYEFEQQRYRSSGLSEAELRDLLALKGSSYNGLLQRYNIHSENVEHIVQSLRKEGTDVRLVKRRDYDEETVRWADAIISAGGDGTMLLAASKVQDRFKPVIGVNTDPERSEGHLCLPVRYTWSFPEALQKLYRGEFRWQWRQRIRLYLEGTGINLTPVDLHEQQLSLEQHNKAHNSQLEQKSVAVSGPQLLPVRALNEVFIGESLSSRVNYKSCKPRFTFSLHRASYYEISVDDGPWEKQKSSGLNVCTGTGSKAWSYNINKMSSQSVEELL... | Function: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor (By similarity).
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 48050
Sequence Length: 427
Subcellular Location: Mitochondrion
EC: 2.7.1.23
|
Q3Z997 | MYKKIGIIYHPLNPAACELAVRLAAKLDSLGIENWSDSAWQADKLASKIQNTQLIVTTGGDGTILRTAHAILPHEIPILSINLGKVGFMTELSPEDAILGLEKVLAGNGWIDERNLLEAEYLPHNSAPARQFFIMNDAVVARGQIARVICVSVDINSHPFTTYKADGAIVSTATGSTGYSYAAGGPVLQPNSADIILTPILPHLGRGYSLVLPADSTIDLKVNTWHEATLSIDGFINMPVSSGDILRLRRSAKKINFIRLRPDNYFYKELDTKLKGNNESVYDR | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31025
Se... |
Q86W26 | MAMAKARKPREALLWALSDLEENDFKKLKFYLRDMTLSEGQPPLARGELEGLIPVDLAELLISKYGEKEAVKVVLKGLKVMNLLELVDQLSHICLHDYREVYREHVRCLEEWQEAGVNGRYNQVLLVAKPSSESPESLACPFPEQELESVTVEALFDSGEKPSLAPSLVVLQGSAGTGKTTLARKMVLDWATGTLYPGRFDYVFYVSCKEVVLLLESKLEQLLFWCCGDNQAPVTEILRQPERLLFILDGFDELQRPFEEKLKKRGLSPKESLLHLLIRRHTLPTCSLLITTRPLALRNLEPLLKQARHVHILGFSEEER... | Function: Inhibits autoprocessing of CASP1, CASP1-dependent IL1B secretion, PYCARD aggregation and PYCARD-mediated apoptosis but not apoptosis induced by FAS or BID . Displays anti-inflammatory activity . Required for immunity against C.albicans infection (By similarity). Involved in the innate immune response by contr... |
A0A6G9KJC3 | MTIANTPAELLASSISTLASRYAEKVQAGENADTEIASIVSACKDLDALVTPPESWNDRMAMSYTISTAIALLLNWDVFQILAAQAKPTSLETLATSCGCSKSLLRCALREAVAHRMLDELSPETYALNSRSSCLLDENKAAWIHYLTDIGLVTAAYLPKYVKSINGKIPEHSHRIALQMAFNVDETFYEFLHRKDPKRGVNFDKAMQRHIKGDAQASIESVFDFSILRPGAVVVDVGGGKGHHCIRIAKKHPHLSFIIQDYEANGPSDGEDTLPEALARRVRWQRHNFHHKQPMDGADVYLLSNILMDNTVSDCNRILT... | Function: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the benzazepine alkaloid nanangelenin A which contains an unprecedented 3,4-dihydro-1-benzazepine-2,5-dione-N-prenyl-N-acetoxy-anthranilamide scaffold . The first step of nanangelenin biosynthesis is catalyzed by the indoleamine 2... |
O51589 | MIIIVKIKRGLIVSCQALENEPLHSSFIMSKMALAAKIGGAIGIRANGVNDISQIKLEVDLPIIGIIKKNYNNCDVFITPTMKEIDELCNEGVDIIALDATFRNRPDGVLLDDFFENIKKKYPKQCLMADISSLDEAINADKLGFDFIGTTLYGYTKNTNGLNIADNDFNFLRTLLNSNLKSTLIVEGKIDTPLKAQKCFEMGVDLVVVGGAITRPAEITKKFVEKINQIKK | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 25644
Sequence Length: 232
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; ... |
Q8R7I7 | MQMDIIQKLENGLIVSCQALEGEPLHSPFIMAKMAKAAEIGGAVAIRANGYEDIVAIKKEVSIPVIGLIKKRYEGYAPYITPTMEEVDKVIEAGADIVAIDATKAYKPGGLTTGEFLKRIKEKYPKILVMADISTYEEGIEAEKLGFDLISTTLSGYTEYSPELEGPDYELIERLARKVNVPIIAEGRIWTPEEAVKALEKGAYAVVVGTAITRPHEITRRFVTFIKERRYSNVRAK | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 26268
Sequence Length: 237
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; ... |
Q0TUP9 | MLDVVKGNLIVSCQALSDEPLHSSFIMGRMAIAAKQGGAAAIRAQGVNDINEIKEVTKLPIIGIIKRNYDDSEIYITPTMKEVDELLKTDCEMIALDATKRKRPNGENVKDLVDAIHAKGRLAMADISTLEEGIEAEKLGFDCVSTTLSGYTPYSKQSNSVDFELLEELVKTVKIPVICEGRINTPEELKKALDLGAYSAVVGGAITRPQQITKRFTDILK | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 24153
Sequence Length: 221
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; ... |
A4QH48 | MDLNTQRSKLYAQLQGQLIVSVQAPDGHAMRDTHTLTHVAAACVDGGAPAIRCGGYGGLEDIRSISNRVDVPVFGLTKEGSEGVYITPTRDSVRAVAESGATVVCADATFRPRPDGSTFAELVTVAHDSGILIMADCATPEEVLSAHKAGADFVSTTLAGYTEHREKTVGPDFDCLREARELVPDAFLIGEGRFSNPADVAHGRLIGANAIIVGTAITDPGFITGQFASLLH | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 24361
Sequence Length: 232
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; ... |
Q6A6A0 | MSGFTDRIIASMAGGLVVSCQAYPGEPLRHPETMAQMAAAVEAGGAVAVRAQGLSDVSAVKGRVSVPVVGIWKEGDEGIYITPTLRHARCVSAAGADVVALDGTRRERADGLSLAETIERLKREYDVVVMADCGSVDDGLFAAEAGADLIGTTLCGYTGERPKTDGPDYEVIEALVKKLDGDRPVIAEGRIHTPDQARRAMDLGAHAVVVGTAITHPTSITGWFRDALR | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 24056
Sequence Length: 229
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; ... |
Q9CKB3 | MRCLALDIGGTKIASAIVTDGKIEQRQQIATPQADAANAMHDTLANILALYAGQFDYVAVASTGIINHGVLTALNPKNLGGLAEFPLKESIARHTDKPIGLLNDVQAAACAEYKDEDKNAVQNFVFITVSTGVGGGIILERRLLTEPNGVAGHIGHTLADPNGPVCGCGRVGCVEAVAAGRAIEAVSSQWNPPCTPKQAFELFRKNDEKATALIQRSASAIANLIADLVIGLDVQKVVVGGSVGLAEGYLPLVKQYLNMMPHFYHCTVEQARHGQDAGLLGAAWWVADCLKQGVHLK | Function: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P.
Catalytic Activity: an N-acyl-D-mannosamine + ATP = ADP + an N-acyl-D-mannosamine 6-phosphate + H(+)
Sequence Mass (Da): 31351
Sequence Length: 297
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosph... |
Q70Z17 | MSNAKDNFNVADLTAALNAEDRDDLVNVLKNKLQGLTGKHSNVLENLSPNVRKRVEVLREIQTQHDELEAKFFEERAALEAKYQKQYQPLYAKRSEIVNGVVEVDGEATQTAAADEEEDKDSVEKGVPDFWVTAMKNNEVLAEEITERDEGALKFLKDIKWSRIENPKGFKLEFFFETNPYFTNTVLTKTYHMIDEDEPILEKAIGTEIEWHPGKCLTQKILKKKPKKGSKNSKPITKIEQCESFFNFFSPPQVPDDEEDIDEDAAEELQNLMEQDYDIGSTIRDKIIPHAVSWFTGEAAQDEDYIDLEDDEDEEDDEDE... | Function: May modulate chromatin structure by regulation of nucleosome assembly/disassembly (By similarity). Could function together with B-type cyclins in the regulation of microtubule dynamics.
Sequence Mass (Da): 43090
Sequence Length: 377
Domain: The acidic domain is probably involved in the interaction with histon... |
F4JEI8 | MSNEENIKSDNKSGDSSDLPTIPALDIGAEECDLLAELKNLTLKRPFDVKKLSPKVTKRVLFLKDIQVTHDELEEKFLAEKSALEATYDNLYKPLFAKRYEIVNGVVEAEAEKEGVPNFWLIAMKTNEMLANEITERDEAALKYLKDIRSCRVEDTSRNFKLEFLFDSNLYFKNSVLSKTYHVNDEDGPVLEKVIGTDIEWFPGKCLTHKVVVKKKTKKGPKKVNNIPMTKTENCESFFNFFKPPEIPEIDEVDDYDDFDTIMTEELQNLMDQDYDIAVTIRDKLIPHAVSWFTGEALVDEDDSDDNDDDDNDEKSD | Function: May modulate chromatin structure by regulation of nucleosome assembly/disassembly.
Sequence Mass (Da): 36418
Sequence Length: 317
Domain: The acidic domain is probably involved in the interaction with histones.
Subcellular Location: Nucleus
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Q55ED1 | MSENNEIEMELPFDSSAITSTEVLDRVNALLTLQDTQNELTEQMEKEILEIEKKYLKKFQPLAEKRFEIVSGKVEPTKEDQQCKAPIQVENLKSVPTDKGIPKFWLHVLQNTEVKDIIEECDIEALEYLVDIKIVQVGDAQDYSLDFHFSENPFFTNTVISKTVKLEEDNELNEIVSTPINWKDGKNFTVQSKKKTVKSKPTKGKAATTTSTTVQEVVPCFFSTFVSPNQDPTSDEEADEIMYIQYQIIAKLKDIVIPEAVNFFLGRASDAEENDYDFGEDFEDEEGEDDDEEDDEEEQTIKKPSGKGKAQPQQPQDCKQ... | Function: May modulate chromatin structure by regulation of histone octamer formation.
Sequence Mass (Da): 36644
Sequence Length: 321
Domain: The acidic domain may be involved in the interaction with histones.
Subcellular Location: Nucleus
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P25293 | MSDPIRTKPKSSMQIDNAPTPHNTPASVLNPSYLKNGNPVRAQAQEQDDKIGTINEEDILANQPLLLQSIQDRLGSLVGQDSGYVGGLPKNVKEKLLSLKTLQSELFEVEKEFQVEMFELENKFLQKYKPIWEQRSRIISGQEQPKPEQIAKGQEIVESLNETELLVDEEEKAQNDSEEEQVKGIPSFWLTALENLPIVCDTITDRDAEVLEYLQDIGLEYLTDGRPGFKLLFRFDSSANPFFTNDILCKTYFYQKELGYSGDFIYDHAEGCEISWKDNAHNVTVDLEMRKQRNKTTKQVRTIEKITPIESFFNFFDPPK... | Function: Acidic protein, which assembles histones into an octamer (in vitro). Involved in the regulation of the localization and the function of the septins during mitosis. Involved in the function of B-type cyclins.
PTM: Phosphorylation by CK2 is required for normal progression through S phase. CK2 phosphorylation is... |
K4BNG7 | MVGKNNSNHLPPGFRFHPTDEELIMYYLRNQATSKPCPSSIIPEVDVYKFDPWELPEKTEFGEKEWYFFTPRDRKYPNGVRPNRAAVSGYWKATGTDKGIYSGTKYVGIKKALVFYKGKPPKGIKTDWIMHEYRLSESRTQPTRPNGSMRLDDWVLCRIYKKKNLERAIEMMKVEEDTQEPQIMSVTNPIHEVVASNGQQTLKLPRTCSLSHLLEMDYFGSISQLFDDNNSYNTISQNNTLMTNVNGYVMPHQAMEKFQLGEVSQISMNPSYQFQ | Function: Transcription factor that binds DNA motifs 5'-CGT[AG](5N)NACG[ACT][AC][AT][ACG][ACT]-3' and 5'-CACG[ACT][AC][AT][AGT][CT]-3' in target genes promoters. Promotes leaf senescence (developmental, light-induced and ABA-induced senescence) and regulates fruit yield and sugar content, probably by establishing absci... |
Q9ZV87 | MGKIMEWAARSDHLGGIPRNTVIMAVSAFAKAVANLCNKSSVHNADTLMNLVQSRPPGVPLITVSNHMSTLDDPVMWGAFKGLLSLDPELARWVLAAEDICFRNPIFSYIFRTGKCIPITRGGGIYQENMNEALQRLKDGSWLHTFPEGKVFQDDVPIRRLKWGTASLIARSPVTPIVLPIIHRGFEEMMPENYNNGRRPLVPLPNKHLKVVVGEPIEFDVPMMVETAVLDSRHVTPPLQEVKWPVLTSAGQVLDETAQRHLYIALSEKIQSSLETLRLLAKRL | Function: Acyltransferase that catalyzes the N-acylation of phosphatidylethanolamine to form N-acylphosphatidylethanolamine (N-acyl-PE) (e.g. NAPEs containing C16:0, C16:1, C18:0, and C18:1). Mediates also the formation of acylphosphatidylglycerol (acyl-PG) from lysoglycerophospholipid by O-acylation. Uses acyl-CoA as ... |
P37062 | MKVIVLGSSHGGYEAVEELLNLHPDAEIQWYEKGDFISFLSCGMQLYLEGKVKDVNSVRYMTGEKMESRGVNVFSNTEITAIQPKEHQVTVKDLVSGEERVENYDKLIISPGAVPFELDIPGKDLDNIYLMRGRQWAIKLKQKTVDPEVNNVVVIGSGYIGIEAAEAFAKAGKKVTVIDILDRPLGVYLDKEFTDVLTEEMEANNITIATGETVERYEGDGRVQKIVTDKNAYDADLVVVAVGVRPNTAWLKGTLELHPNGLIKTDEYMRTSEPDVFAVGDATLIKYNPADTEVNIALATNARKQGRFAVKNLEEPVKPF... | Cofactor: Binds 1 FAD per subunit.
Function: Peroxidase whose active site is a redox-active cysteine-sulfenic acid.
Catalytic Activity: H(+) + H2O2 + NADH = 2 H2O + NAD(+)
Sequence Mass (Da): 49566
Sequence Length: 447
EC: 1.11.1.1
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Q56348 | MIDSAKETDRPKHRKRDEVIAFLILAVVIWPILSVAIVGGYGFLVWMSQIIFGPPGPMH | Function: May be involved in mediating interactions between NapC and a quinol oxidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6618
Sequence Length: 59
Subcellular Location: Cell inner membrane
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P0AAL2 | MKIDASRRGILTGRWRKASNGIRPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPESLFSPRHTRAWDLQFTIGDACLAYQSVECRRCQDSCEPMAIIFRPTLSGIYQPQLNSQLCNGCGACAASCPVSAITAEYLHAH | Cofactor: Binds 3 [4Fe-4S] cluster.
Function: Could be involved in the maturation of NapA, the catalytic subunit of the periplasmic nitrate reductase, before its export into the periplasm.
Sequence Mass (Da): 18047
Sequence Length: 164
Subcellular Location: Cytoplasm
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P44650 | MTVENLPRRQFLRGKFSTLSCLENNQKQNFVGIRPPWSVENSIFVARCTRCGDCLSVCETNILVKGDAGFPEVRFDNGECTFCGKCVDACKQPIFYPRDQLPWSHKIDISVSCLTLHRIECRTCQDNCPANAIRFKLQMGGVAQPLVNFDACNGCGACVQGCPVNAITMNDLKQNE | Cofactor: Binds 4 [4Fe-4S] clusters or perhaps rather 3 [4Fe-4S] clusters and 1 3Fe-4S cluster, leaving Cys-113 out of the cluster ligands.
Function: Could be involved in the maturation of NapA, the catalytic subunit of the periplasmic nitrate reductase, before its export into the periplasm.
Sequence Mass (Da): 19604
S... |
P0AAL4 | MSRSAKPQNGRRRFLRDVVRTAGGLAAVGVALGLQQQTARASGVRLRPPGAINENAFASACVRCGQCVQACPYDTLKLATLASGLSAGTPYFVARDIPCEMCEDIPCAKVCPSGALDREIESIDDARMGLAVLVDQENCLNFQGLRCDVCYRECPKIDEAITLELERNTRTGKHARFLPTVHSDACTGCGKCEKVCVLEQPAIKVLPLSLAKGELGHHYRFGWLEGNNGKS | Cofactor: Binds 4 [4Fe-4S] cluster.
Function: Required for electron transfer from ubiquinol, via NapC, to the periplasmic nitrate reductase NapAB complex.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 24925
Sequence L... |
P44652 | MKVRLKSKKKMKKPALNPERRKFLKEATRTAGGLAGVGILLGLQQNQSLAREGVPLRPPFALQDAKAFSAACIRCGQCVQACPYDMLHLASLLSPVEAGTPYFIARDKPCEMCPDIPCAKACPSGALDRQATDINESRMGLSVLLDHETCLNYQGLRCDVCYRVCPLIDKAITLETQHNPRSDKHALFIPTVHSDACTGCGKCEQACVLEEAAIKILPMDLAKGMLGKHYRLGWEEKAKAGHSLAPKDMISLPTRTPEGTTVIPEPAEPVLAPILGSGK | Cofactor: Binds 4 [4Fe-4S] cluster.
Function: Required for electron transfer from ubiquinol, via NapC, to the periplasmic nitrate reductase NapAB complex.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 30227
Sequence L... |
P33934 | MANRKRDAGREALEKKGWWRSHRWLVLRRLCQFFVLGMFLSGPWFGVWILHGNYSSSLLFDTVPLTDPLMTLQSLASGHLPATVALTGAVIITVLYALAGKRLFCSWVCPLNPITDLANWLRRRFDLNQSATIPRHIRYVLLVVILVGSALTGTLIWEWINPVSLMGRSLVMGFGSGALLILALFLFDLLVVEHGWCGHICPVGALYGVLGSKGVITVAATDRQKCNRCMDCFHVCPEPHVLRAPVLDEQSPVQVTSRDCMTCGRCVDVCSEDVFTITTRWSSGAKS | Cofactor: Binds 2 [4Fe-4S] cluster.
Function: Required for electron transfer from ubiquinol, via NapC, to the periplasmic nitrate reductase NapAB complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31874
Sequence Length: 287
Subcellular Location: Cell inner membrane
|
O96009 | MSPPPLLQPLLLLLPLLNVEPSGATLIRIPLHRVQPGRRILNLLRGWREPAELPKLGAPSPGDKPIFVPLSNYRDVQYFGEIGLGTPPQNFTVAFDTGSSNLWVPSRRCHFFSVPCWLHHRFDPKASSSFQANGTKFAIQYGTGRVDGILSEDKLTIGGIKGASVIFGEALWEPSLVFAFAHFDGILGLGFPILSVEGVRPPMDVLVEQGLLDKPVFSFYLNRDPEEPDGGELVLGGSDPAHYIPPLTFVPVTVPAYWQIHMERVKVGPGLTLCAKGCAAILDTGTSLITGPTEEIRALHAAIGGIPLLAGEYIILCSEI... | Function: May be involved in processing of pneumocyte surfactant precursors.
Sequence Mass (Da): 45387
Sequence Length: 420
Subcellular Location: Secreted
EC: 3.4.23.-
|
Q9N2V2 | MRISSLLFLTFLAGIVQAQDFLAMFKPFLGGGGGGGNPFANPQAIGGLFQQFAGGNGGGFGQLLAGAMAPKPAPAAAGPRSAPAPTNEDYNTDIDVPAPKAKARAAPTPRRAQADAPPVYRQPRTKAEKIERFRNIARTFSPFVYEVNTTPAPHFDNFIWQQNAPAVTPEPFTFAPFSFPTLATVAPPAPGPGGPTLEPFLPTTASPKLLAHNTARMIREIASFSDGGRSRDQDFGAVQTLMQAFFEAVSSGNNGGAGAAAGAGTALGDAPMLQAHRDGTELGANRALTNKLFESDMVLTVKQMKAIVLAAQEARNPHGR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 80722
Sequence Length: 741
EC: 3.4.24.-
|
Q7JLI1 | MILQLLFYSLFTHLAVSQIDVNQALNQNKLNIDTISSSAISDAELEKTFPRTNLSRMRNALKSLRQNWSAKLQAMPARNYQNAGTNQENGATEQQKPLREKPRDRVKMEGDTLHQVNKAAGLNDILYQGDMVLTDDQIATILEARDETTVSTASRARRQAYRDRYYPSTTWGSSVYYYYDRTATPKIVKAFEQAVAFWQNVTCINIMQSSTAINRIRVFKGQGCYSYVGRISGVQDLSLGTGCEEFGTAAHELGHALGFFHTQSRYDRDNYISINYANIDPSYVEQFDKETSNTNFNYGMPYDYGSIMQYGATSASSNDK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 68854
Sequence Length: 611
Subcellular Location: Secreted
EC: 3.4.24.-
|
O16977 | MRRFFICYIGFLSIFLDFILADKDNNSEEERDRKFDWKFENENGKPEHETVTVPKLPDGSYFWKWTWNSRINSTTAATPTSTVTTSTSAPTTSPRVYKLKSEARKSLRKALRGVPPEKRKKQLKKMGKKMMKIPKITKKESNKLHKSYRKVKITENPPALDMFEVNERAGLNEYLFQGDINLNNNQIAKISSEQSSKSRRKKRQIDNLAQFWPGKVVYYYFDSGLTTTVQQIVRDAITFLESNTCLKFELNSTATNRIFSGVGCYSDTGMLGGEQTLSLGYGCEVTGTAAHEIAHTLGLFHTQMRSDRDDYVTIDLTDVP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 72761
Sequence Length: 651
Subcellular Location: Secreted
EC: 3.4.24.-
|
P55114 | MLFVSILISQFVTCLTQPDFFERPPPPDWFFPGPLRPWGPPPPWHRNRGPPPFGPPPPWDRPPPPWRRPPWHRRPPWGLPPPPPPPEPEPQQDQPQVMFSQDIDKVVNSVNQNTAAFQRPGESYDKVIQIMSSYFNRKSGSQYDINTVIPSSGIYNNEMAANSKIAAVMFESDMALTVSQMNKVAQNGFRVKRKMNLNGTTWSRNIPYRFLDTDGNWQSQITNGLRHYERNTCIRFSLNGGGSDYLVFSKGEGCYSSVGRLGGPQEISIGDGCETLGIITHEVGHALGFWHEQARPERDSYVRINRQNAINGLEGQFDKR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 72526
Sequence Length: 644
Subcellular Location: Secreted
EC: 3.4.24.-
|
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